scholarly journals The crystal structure of mammalian inositol 1,3,4,5,6-pentakisphosphate 2-kinase reveals a new zinc-binding site and key features for protein function

2017 ◽  
Vol 292 (25) ◽  
pp. 10534-10548 ◽  
Author(s):  
Elsa Franco-Echevarría ◽  
Julia Sanz-Aparicio ◽  
Charles A. Brearley ◽  
Juana M. González-Rubio ◽  
Beatriz González
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Protein Function ◽  
Zinc Binding ◽  
Zinc Binding Site ◽  
Key Features

scholarly journals Crystal structure of the DENR-MCT-1 complex revealed zinc-binding site essential for heterodimer formation

2018 ◽  
Vol 116 (2) ◽  
pp. 528-533 ◽  
Author(s):  
Ivan B. Lomakin ◽  
Sergey E. Dmitriev ◽  
Thomas A. Steitz
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Translation Initiation ◽  
Zinc Ion ◽  
Zinc Binding ◽  
Ion Binding ◽  
Binding Interface ◽  
Zinc Binding Site ◽  
Reading Frames ◽  
Zinc Ion Binding

The density-regulated protein (DENR) and the malignant T cell-amplified sequence 1 (MCT-1/MCTS1) oncoprotein support noncanonical translation initiation, promote translation reinitiation on a specific set of mRNAs with short upstream reading frames, and regulate ribosome recycling. DENR and MCT-1 form a heterodimer, which binds to the ribosome. We determined the crystal structure of the heterodimer formed by human MCT-1 and the N-terminal domain of DENR at 2.0-Å resolution. The structure of the heterodimer reveals atomic details of the mechanism of DENR and MCT-1 interaction. Four conserved cysteine residues of DENR (C34, C37, C44, C53) form a classical tetrahedral zinc ion-binding site, which preserves the structure of the DENR’s MCT-1–binding interface that is essential for the dimerization. Substitution of all four cysteines by alanine abolished a heterodimer formation. Our findings elucidate further the mechanism of regulation of DENR-MCT-1 activities in unconventional translation initiation, reinitiation, and recycling.

Crystal Structure of Streptococcus dysgalactiae-Derived Mitogen Reveals a Zinc-Binding Site and Alterations in TcR Binding

2007 ◽  
Vol 373 (5) ◽  
pp. 1089-1097 ◽  
Author(s):  
Susanna Saarinen ◽  
Hidehito Kato ◽  
Takehiko Uchiyama ◽  
Tohru Miyoshi-Akiyama ◽  
Anastassios C. Papageorgiou
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Zinc Binding ◽  
Streptococcus Dysgalactiae ◽  
Zinc Binding Site

scholarly journals The Crystal Structure of Hepatitis C Virus NS3 Proteinase Reveals a Trypsin-like Fold and a Structural Zinc Binding Site

Cell ◽  
1996 ◽  
Vol 87 (2) ◽  
pp. 331-342 ◽  
Author(s):  
Robert A Love ◽  
Hans E Parge ◽  
John A Wickersham ◽  
Zdenek Hostomsky ◽  
Noriyuki Habuka ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Binding Site ◽  
Zinc Binding ◽  
Zinc Binding Site

scholarly journals Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site

Structure ◽  
1995 ◽  
Vol 3 (8) ◽  
pp. 769-779 ◽  
Author(s):  
Anastassios C Papageorgiou ◽  
K.Ravi Acharya ◽  
Robert Shapiro ◽  
Edward F Passalacqua ◽  
Rossalyn D Brehm ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Staphylococcus Aureus ◽  
Binding Site ◽  
Zinc Binding ◽  
Zinc Binding Site

Crystal Structure of a Zinc-Activated Variant of Human Carbonic Anhydrase I, CA I Michigan 1:  Evidence for a Second Zinc Binding Site Involving Arginine Coordination

Biochemistry ◽  
2002 ◽  
Vol 41 (20) ◽  
pp. 6237-6244 ◽  
Author(s):  
Marta Ferraroni ◽  
Silvia Tilli ◽  
Fabrizio Briganti ◽  
W. Richard Chegwidden ◽  
Claudiu T. Supuran ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Carbonic Anhydrase ◽  
Binding Site ◽  
Zinc Binding ◽  
Carbonic Anhydrase I ◽  
Zinc Binding Site ◽  
Human Carbonic Anhydrase

Crystal structure of active site mutant of antileukemicl-asparaginase reveals conserved zinc-binding site

FEBS Journal ◽  
2014 ◽  
Vol 281 (18) ◽  
pp. 4097-4111 ◽  
Author(s):  
Dominika Borek ◽  
Maciej Kozak ◽  
Jimin Pei ◽  
Mariusz Jaskolski
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Active Site ◽  
Zinc Binding ◽  
Zinc Binding Site

Effect of the hydrogen bond network in carbonic anhydrase II zinc binding site. A theoretical study

1998 ◽  
Vol 76 (7) ◽  
pp. 1027-1032 ◽  
Author(s):  
Silvia Álvarez-Santos ◽  
Àngels González-Lafont ◽  
José M Lluch
Keyword(s):  
Hydrogen Bond ◽  
Carbonic Anhydrase ◽  
Binding Site ◽  
Zinc Binding ◽  
Carbonic Anhydrase Ii ◽  
Am1 Method ◽  
Hydrogen Bond Network ◽  
Zinc Binding Site ◽  
Bond Network ◽  
Metal Ligand

The hydrogen bond network influence on the carbonic anhydrase II (CAII) zinc binding site has been studied theoretically by using the semiempirical AM1 method. To this aim, quantum mechanical reduced models of wild-type CAII and several CAII variants have been constructed. We have shown that, when a direct metal ligand donates a hydrogen bond to an indirect metal ligand, the first-shell residues enhance their electrostatic interaction with the zinc cation. Thus, the hydrogen-bond network is able to modulate the zinc binding affinity and the zinc-water pKa.Key words: hydrogen bond network, carbonic anhydrase II, Zn2+ metalloenzyme ligands.

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